作者
Loren Lasko,Clarissa G. Jakob,Rohinton Edalji,Wei Qiu,Debra Montgomery,Enrico L. DiGiammarino,T. Matt Hansen,Roberto M. Risi,Robin R. Frey,Vlasios Manaves,Bailin Shaw,Mikkel A. Algire,Paul Hessler,Lloyd T. Lam,Tamar Uziel,Emily J. Faivre,Debra C. Ferguson,Fritz G. Buchanan,Ruth L. Martin,Maricel Torrent,Gary G. Chiang,Kannan R. Karukurichi,J. William Langston,Brian T. Weinert,Chunaram Choudhary,Peter de Vries,Arthur F. Kluge,Michael A. Patane,John H. Van Drie,Ce Wang,David McElligott,Ed Kesicki,Ronen Marmorstein,Chaohong Sun,Philip A. Cole,Saul H. Rosenberg,Michael R. Michaelides,Albert Lai,Kenneth D. Bromberg
摘要
A potent and selective catalytic inhibitor of p300/CBP histone acetyltransferases suppresses tumour proliferation across multiple cell lineages, illustrating the therapeutic potential of drug-like small molecules that target histone acetyltransferases. The dynamic and reversible acetylation of proteins, catalysed by histone acetyltransferases (HATs) and histone deacetylases (HDACs), is a major epigenetic regulatory mechanism of gene transcription1 and is associated with multiple diseases. Histone deacetylase inhibitors are currently approved to treat certain cancers, but progress on the development of drug-like histone actyltransferase inhibitors has lagged behind2. The histone acetyltransferase paralogues p300 and CREB-binding protein (CBP) are key transcriptional co-activators that are essential for a multitude of cellular processes, and have also been implicated in human pathological conditions (including cancer3). Current inhibitors of the p300 and CBP histone acetyltransferase domains, including natural products4, bi-substrate analogues5 and the widely used small molecule C6466,7, lack potency or selectivity. Here, we describe A-485, a potent, selective and drug-like catalytic inhibitor of p300 and CBP. We present a high resolution (1.95 Å) co-crystal structure of a small molecule bound to the catalytic active site of p300 and demonstrate that A-485 competes with acetyl coenzyme A (acetyl-CoA). A-485 selectively inhibited proliferation in lineage-specific tumour types, including several haematological malignancies and androgen receptor-positive prostate cancer. A-485 inhibited the androgen receptor transcriptional program in both androgen-sensitive and castration-resistant prostate cancer and inhibited tumour growth in a castration-resistant xenograft model. These results demonstrate the feasibility of using small molecule inhibitors to selectively target the catalytic activity of histone acetyltransferases, which may provide effective treatments for transcriptional activator-driven malignancies and diseases.